The Study of Protein Conformation in Solution Via Direct Sampling by Desorption Electrospray Ionization Mass Spectrometry

Zhixin Miao, Shiyong Wu, Hao Chen

Research output: Contribution to journalArticlepeer-review

42 Scopus citations

Abstract

The direct sampling feature of liquid sample desorption electrospray ionization (DESI) allows the ionization of liquid samples without adding acids/organic solvents (i.e., without sample pretreatment). As a result, it provides a new approach for probing protein conformation in solution. In this study, it has been observed that native protein ions are generated from proteins in water by DESI. Interestingly, the intensities of the resulting protein ions appear to be higher than those generated by ESI of the proteins in water or in ammonium acetate. For protein solutions that already contain acids/organic solvents, DESI can be used to investigate the influences of these denaturants on protein conformations and the obtained results are in good agreement with spectroscopic data. In addition, online monitoring of protein conformational changes by DESI is feasible; for instance, heat-induced unfolding of ubiquitin can be traced with DESI in water without influences of organic solvents/acids. This DESI method provides a new alternative tool for the study of protein conformation in solution.

Original languageEnglish (US)
Pages (from-to)1730-1736
Number of pages7
JournalJournal of the American Society for Mass Spectrometry
Volume21
Issue number10
DOIs
StatePublished - Oct 2010
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Spectroscopy

Fingerprint Dive into the research topics of 'The Study of Protein Conformation in Solution Via Direct Sampling by Desorption Electrospray Ionization Mass Spectrometry'. Together they form a unique fingerprint.

Cite this